We are analyzing https://link.springer.com/article/10.1007/bf00964867.

Title:
Iron-induced lipid peroxidation and inhibition of dopamine synthesis in striatum synaptosomes | Neurochemical Research
Description:
Crude striatum synaptosomes (P2 fraction) from Fisher 344 female rats were incubated in the presence of ADP-chelated Fe3+ (0.5–50 μM) and ascorbate (250 μM). Intrasynaptosomal conversion of tyrosine to dopamine (DA) was measured by14CO2 evolution froml-[1-14C]tyrosine in the absence of added cofactors and DOPA decarboxylase. Malondialdehyde (MDA) was measured as an index of lipid peroxidation. A concentration-dependent inhibition of DA synthesis by ADP-Fe3+/ascorbate was found with 50% inhibition occurring at 2.5 μM Fe3+ concentration. This was accompanied by marked accumulation of MDA. Ascorbate or ADP alone did not affect DA synthesis and ADP-Fe3+ in the absence of exogenous ascorbate was effective only above 25 μM. Exogenously added MDA did not inhibit DA synthesis. Purified synaptosomes were isolated from peroxidized and control P2 fractions using sucrose gradients. Membrane microviscosity of the purifled synaptosomes was assessed by nitroxyl spin labels of stearic acid using electron paramagetic resonance techniques. There was a significant increase in membrane microviscosity as a result of ADP-Fe3+/ascorbate induced peroxidation. Maleimide nitroxide spin-label binding to protein sulhydryls was significantly modified by peroxidation of striatum synaptosomes. The weakly immobilized component of the sulhydryl spin-label (w) was drastically decreased whereas the strongly immobilized component (s) was modified less, thus leading to a marked reduction of w/s ratio. The exposure of striatum synaptosomes to the peroxidizing system resulted in a significant increase in total iron and in a 25% decrease in protein sulhydryl content. It is concluded that ironinduced damage to the DA synthetic system is mediated by alterations of the structural properties of nerve ending membranes.
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Topics {✒️}

month download article/chapter adp-fe3+/ascorbate induced peroxidation γ-aminobutyric acid uptake iron-induced lipid peroxidation superoxide radical-mediated alteration ferrous iron-nucleotide complexes lipid peroxidation-induced inhibition ascorbic acid-stimulated peroxidation γ-aminobutyric acid iron-induced damage privacy choices/manage cookies lipid peroxidation damage full article pdf regional lipid peroxidation rat brain cortex cellular edema induced sulhydryl spin-label free-radical mechanisms electron-microscopic study dopamine biosynthetic system oxygen free radical nitroxyl spin labels unsaturated fatty acids spin label studies lipid peroxides mechanism thiobarbituric acid reactivity striatal synaptosomes exposed mammalian cortical neurons concentration-dependent inhibition dopamine receptor stimulation rat striatal synaptosomes european economic area adp-chelated fe3+ weakly immobilized component strongly immobilized component peroxidizing system resulted reducible disulfide proteome neurobehavioral motor deficits histopathological biomarkers relevant atp-ase activity dopaminergic nigrostriatal perikarya c57bl/6nna mouse thiobarbituric acid reagent prolonged cardiac arrest university medical school rat liver mitochondria conditions privacy policy folin phenol reagent reactive oxygen species control p2 fractions

Schema {🗺️}

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         headline:Iron-induced lipid peroxidation and inhibition of dopamine synthesis in striatum synaptosomes
         description:Crude striatum synaptosomes (P2 fraction) from Fisher 344 female rats were incubated in the presence of ADP-chelated Fe3+ (0.5–50 μM) and ascorbate (250 μM). Intrasynaptosomal conversion of tyrosine to dopamine (DA) was measured by14CO2 evolution froml-[1-14C]tyrosine in the absence of added cofactors and DOPA decarboxylase. Malondialdehyde (MDA) was measured as an index of lipid peroxidation. A concentration-dependent inhibition of DA synthesis by ADP-Fe3+/ascorbate was found with 50% inhibition occurring at 2.5 μM Fe3+ concentration. This was accompanied by marked accumulation of MDA. Ascorbate or ADP alone did not affect DA synthesis and ADP-Fe3+ in the absence of exogenous ascorbate was effective only above 25 μM. Exogenously added MDA did not inhibit DA synthesis. Purified synaptosomes were isolated from peroxidized and control P2 fractions using sucrose gradients. Membrane microviscosity of the purifled synaptosomes was assessed by nitroxyl spin labels of stearic acid using electron paramagetic resonance techniques. There was a significant increase in membrane microviscosity as a result of ADP-Fe3+/ascorbate induced peroxidation. Maleimide nitroxide spin-label binding to protein sulhydryls was significantly modified by peroxidation of striatum synaptosomes. The weakly immobilized component of the sulhydryl spin-label (w) was drastically decreased whereas the strongly immobilized component (s) was modified less, thus leading to a marked reduction of w/s ratio. The exposure of striatum synaptosomes to the peroxidizing system resulted in a significant increase in total iron and in a 25% decrease in protein sulhydryl content. It is concluded that ironinduced damage to the DA synthetic system is mediated by alterations of the structural properties of nerve ending membranes.
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      headline:Iron-induced lipid peroxidation and inhibition of dopamine synthesis in striatum synaptosomes
      description:Crude striatum synaptosomes (P2 fraction) from Fisher 344 female rats were incubated in the presence of ADP-chelated Fe3+ (0.5–50 μM) and ascorbate (250 μM). Intrasynaptosomal conversion of tyrosine to dopamine (DA) was measured by14CO2 evolution froml-[1-14C]tyrosine in the absence of added cofactors and DOPA decarboxylase. Malondialdehyde (MDA) was measured as an index of lipid peroxidation. A concentration-dependent inhibition of DA synthesis by ADP-Fe3+/ascorbate was found with 50% inhibition occurring at 2.5 μM Fe3+ concentration. This was accompanied by marked accumulation of MDA. Ascorbate or ADP alone did not affect DA synthesis and ADP-Fe3+ in the absence of exogenous ascorbate was effective only above 25 μM. Exogenously added MDA did not inhibit DA synthesis. Purified synaptosomes were isolated from peroxidized and control P2 fractions using sucrose gradients. Membrane microviscosity of the purifled synaptosomes was assessed by nitroxyl spin labels of stearic acid using electron paramagetic resonance techniques. There was a significant increase in membrane microviscosity as a result of ADP-Fe3+/ascorbate induced peroxidation. Maleimide nitroxide spin-label binding to protein sulhydryls was significantly modified by peroxidation of striatum synaptosomes. The weakly immobilized component of the sulhydryl spin-label (w) was drastically decreased whereas the strongly immobilized component (s) was modified less, thus leading to a marked reduction of w/s ratio. The exposure of striatum synaptosomes to the peroxidizing system resulted in a significant increase in total iron and in a 25% decrease in protein sulhydryl content. It is concluded that ironinduced damage to the DA synthetic system is mediated by alterations of the structural properties of nerve ending membranes.
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